SPART_HUMAN
ID SPART_HUMAN Reviewed; 666 AA.
AC Q8N0X7; O60349; Q86Y67; Q9H1T2; Q9H1T3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Spartin {ECO:0000305};
DE AltName: Full=Spastic paraplegia 20 protein;
DE AltName: Full=Trans-activated by hepatitis C virus core protein 1;
GN Name=SPART {ECO:0000312|HGNC:HGNC:18514};
GN Synonyms=KIAA0610, SPG20 {ECO:0000312|HGNC:HGNC:18514}, TAHCCP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND INVOLVEMENT IN SPG20.
RX PubMed=12134148; DOI=10.1038/ng937;
RA Patel H., Cross H., Proukakis C., Hershberger R., Bork P., Ciccarelli F.D.,
RA Patton M.A., McKusick V.A., Crosby A.H.;
RT "SPG20 is mutated in Troyer syndrome, an hereditary spastic paraplegia.";
RL Nat. Genet. 31:347-348(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RA Liu Y., Cheng J., Wang G., Dong J., Li K., Li L., Zhang L.;
RT "Identification of the genomic DNA structure for a gene trans-activated by
RT hepatitis C virus core protein 1.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP DOMAIN MIT, AND PROBABLE FUNCTION.
RX PubMed=12676568; DOI=10.1016/s0888-7543(03)00011-9;
RA Ciccarelli F.D., Proukakis C., Patel H., Cross H., Azam S., Patton M.A.,
RA Bork P., Crosby A.H.;
RT "The identification of a conserved domain in both spartin and spastin,
RT mutated in hereditary spastic paraplegia.";
RL Genomics 81:437-441(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP UBIQUITINATION, SUBCELLULAR LOCATION, INTERACTION WITH ITCH AND WWP1, AND
RP MUTAGENESIS OF 171-PRO--TYR-174.
RX PubMed=19580544; DOI=10.1042/bj20082398;
RA Edwards T.L., Clowes V.E., Tsang H.T., Connell J.W., Sanderson C.M.,
RA Luzio J.P., Reid E.;
RT "Endogenous spartin (SPG20) is recruited to endosomes and lipid droplets
RT and interacts with the ubiquitin E3 ligases AIP4 and AIP5.";
RL Biochem. J. 423:31-39(2009).
RN [10]
RP INTERACTION WITH IST1, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-24, AND
RP FUNCTION.
RX PubMed=20719964; DOI=10.1091/mbc.e09-10-0879;
RA Renvoise B., Parker R.L., Yang D., Bakowska J.C., Hurley J.H.,
RA Blackstone C.;
RT "SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1
RT and participates in cytokinesis.";
RL Mol. Biol. Cell 21:3293-3303(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP STRUCTURE BY NMR OF 8-111.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the MIT domain from human spartin.";
RL Submitted (OCT-2006) to the PDB data bank.
RN [17]
RP VARIANT SPG20 VAL-330, AND CHARACTERIZATION OF VARIANT SPG20 VAL-330.
RX PubMed=27539578; DOI=10.1007/8904_2016_580;
RA Spiegel R., Soiferman D., Shaag A., Shalev S., Elpeleg O., Saada A.;
RT "Novel homozygous missense mutation in SPG20 gene results in Troyer
RT syndrome associated with mitochondrial cytochrome c oxidase deficiency.";
RL JIMD Rep. 33:55-60(2017).
RN [18]
RP VARIANT SPG20 PRO-442.
RX PubMed=28875386; DOI=10.1007/s11011-017-0104-3;
RA Bizzari S., Hamzeh A.R., Nair P., Mohamed M., Saif F., Aithala G.,
RA Al-Ali M.T., Bastaki F.;
RT "Novel SPG20 mutation in an extended family with Troyer syndrome.";
RL Metab. Brain Dis. 32:2155-2159(2017).
CC -!- FUNCTION: May be implicated in endosomal trafficking, or microtubule
CC dynamics, or both. Participates in cytokinesis (PubMed:20719964).
CC {ECO:0000269|PubMed:20719964}.
CC -!- SUBUNIT: Interacts with ITCH and WWP1 (PubMed:19580544). Interacts (via
CC MIT domain) with IST1; leading to the recruitment of SPART to midbodies
CC (PubMed:20719964). {ECO:0000269|PubMed:19580544,
CC ECO:0000269|PubMed:20719964}.
CC -!- INTERACTION:
CC Q8N0X7; Q9BSY9: DESI2; NbExp=3; IntAct=EBI-2643803, EBI-12878374;
CC Q8N0X7; O95208-2: EPN2; NbExp=3; IntAct=EBI-2643803, EBI-12135243;
CC Q8N0X7; O00291: HIP1; NbExp=3; IntAct=EBI-2643803, EBI-473886;
CC Q8N0X7; P13473-2: LAMP2; NbExp=3; IntAct=EBI-2643803, EBI-21591415;
CC Q8N0X7; Q96DC9: OTUB2; NbExp=3; IntAct=EBI-2643803, EBI-746259;
CC Q8N0X7; Q6GQQ9: OTUD7B; NbExp=3; IntAct=EBI-2643803, EBI-527784;
CC Q8N0X7; Q96BN8: OTULIN; NbExp=3; IntAct=EBI-2643803, EBI-750730;
CC Q8N0X7; P10644: PRKAR1A; NbExp=3; IntAct=EBI-2643803, EBI-476431;
CC Q8N0X7; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-2643803, EBI-14093916;
CC Q8N0X7; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-2643803, EBI-2623095;
CC Q8N0X7; Q9BSL1: UBAC1; NbExp=3; IntAct=EBI-2643803, EBI-749370;
CC Q8N0X7; P45974-2: USP5; NbExp=3; IntAct=EBI-2643803, EBI-12072186;
CC Q8N0X7; Q5VVQ6: YOD1; NbExp=3; IntAct=EBI-2643803, EBI-2510804;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19580544}. Midbody
CC {ECO:0000269|PubMed:20719964}. Note=Transiently associated with
CC endosomes (PubMed:19580544). Colocalized with IST1 to the ends of
CC Flemming bodies during cytokinesis (PubMed:20719964).
CC {ECO:0000269|PubMed:19580544, ECO:0000269|PubMed:20719964}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels of
CC expression detected in adipose tissue.
CC -!- PTM: Ubiquitinated; ubiquitination does not require ITCH and WWP1.
CC {ECO:0000269|PubMed:19580544}.
CC -!- DISEASE: Spastic paraplegia 20, autosomal recessive (SPG20)
CC [MIM:275900]: A form of spastic paraplegia, a neurodegenerative
CC disorder characterized by a slow, gradual, progressive weakness and
CC spasticity of the lower limbs. Rate of progression and the severity of
CC symptoms are quite variable. Initial symptoms may include difficulty
CC with balance, weakness and stiffness in the legs, muscle spasms, and
CC dragging the toes when walking. In some forms of the disorder, bladder
CC symptoms (such as incontinence) may appear, or the weakness and
CC stiffness may spread to other parts of the body. SPG20 is characterized
CC by dysarthria, distal amyotrophy, mild developmental delay and short
CC stature. {ECO:0000269|PubMed:12134148, ECO:0000269|PubMed:27539578,
CC ECO:0000269|PubMed:28875386}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA25536.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY123329; AAM76671.1; -; mRNA.
DR EMBL; AY123337; AAM76672.1; -; Genomic_DNA.
DR EMBL; AY123331; AAM76672.1; JOINED; Genomic_DNA.
DR EMBL; AY123332; AAM76672.1; JOINED; Genomic_DNA.
DR EMBL; AY123333; AAM76672.1; JOINED; Genomic_DNA.
DR EMBL; AY123334; AAM76672.1; JOINED; Genomic_DNA.
DR EMBL; AY123335; AAM76672.1; JOINED; Genomic_DNA.
DR EMBL; AY123336; AAM76672.1; JOINED; Genomic_DNA.
DR EMBL; AY038934; AAK71883.1; -; Genomic_DNA.
DR EMBL; AY038359; AAK72374.1; -; mRNA.
DR EMBL; AB011182; BAA25536.1; ALT_INIT; mRNA.
DR EMBL; AL139377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC047083; AAH47083.1; -; mRNA.
DR CCDS; CCDS9356.1; -.
DR PIR; T00255; T00255.
DR RefSeq; NP_001135766.1; NM_001142294.1.
DR RefSeq; NP_001135767.1; NM_001142295.1.
DR RefSeq; NP_001135768.1; NM_001142296.1.
DR RefSeq; NP_055902.1; NM_015087.4.
DR RefSeq; XP_005266370.1; XM_005266313.4.
DR RefSeq; XP_005266371.1; XM_005266314.3.
DR RefSeq; XP_005266372.1; XM_005266315.3.
DR RefSeq; XP_005266374.1; XM_005266317.3.
DR RefSeq; XP_011533314.1; XM_011535012.2.
DR PDB; 2DL1; NMR; -; A=9-111.
DR PDB; 4U7I; X-ray; 1.79 A; A=8-101.
DR PDBsum; 2DL1; -.
DR PDBsum; 4U7I; -.
DR AlphaFoldDB; Q8N0X7; -.
DR SMR; Q8N0X7; -.
DR BioGRID; 116734; 77.
DR IntAct; Q8N0X7; 56.
DR MINT; Q8N0X7; -.
DR STRING; 9606.ENSP00000414147; -.
DR GlyGen; Q8N0X7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N0X7; -.
DR PhosphoSitePlus; Q8N0X7; -.
DR SwissPalm; Q8N0X7; -.
DR BioMuta; SPART; -.
DR DMDM; 50401600; -.
DR EPD; Q8N0X7; -.
DR jPOST; Q8N0X7; -.
DR MassIVE; Q8N0X7; -.
DR MaxQB; Q8N0X7; -.
DR PaxDb; Q8N0X7; -.
DR PeptideAtlas; Q8N0X7; -.
DR PRIDE; Q8N0X7; -.
DR ProteomicsDB; 71485; -.
DR Antibodypedia; 42112; 207 antibodies from 31 providers.
DR DNASU; 23111; -.
DR Ensembl; ENST00000355182.8; ENSP00000347314.4; ENSG00000133104.14.
DR Ensembl; ENST00000438666.7; ENSP00000406061.2; ENSG00000133104.14.
DR Ensembl; ENST00000451493.5; ENSP00000414147.1; ENSG00000133104.14.
DR Ensembl; ENST00000494062.2; ENSP00000473599.1; ENSG00000133104.14.
DR Ensembl; ENST00000650221.1; ENSP00000497209.1; ENSG00000133104.14.
DR GeneID; 23111; -.
DR KEGG; hsa:23111; -.
DR MANE-Select; ENST00000438666.7; ENSP00000406061.2; NM_015087.5; NP_055902.1.
DR UCSC; uc001uvm.4; human.
DR CTD; 23111; -.
DR DisGeNET; 23111; -.
DR GeneCards; SPART; -.
DR GeneReviews; SPART; -.
DR HGNC; HGNC:18514; SPART.
DR HPA; ENSG00000133104; Low tissue specificity.
DR MalaCards; SPART; -.
DR MIM; 275900; phenotype.
DR MIM; 607111; gene.
DR neXtProt; NX_Q8N0X7; -.
DR OpenTargets; ENSG00000133104; -.
DR Orphanet; 101000; Autosomal recessive spastic paraplegia type 20.
DR PharmGKB; PA134871645; -.
DR VEuPathDB; HostDB:ENSG00000133104; -.
DR eggNOG; KOG2709; Eukaryota.
DR GeneTree; ENSGT00390000012235; -.
DR HOGENOM; CLU_019310_0_0_1; -.
DR InParanoid; Q8N0X7; -.
DR OMA; VCSIANC; -.
DR OrthoDB; 650471at2759; -.
DR PhylomeDB; Q8N0X7; -.
DR TreeFam; TF105252; -.
DR PathwayCommons; Q8N0X7; -.
DR SignaLink; Q8N0X7; -.
DR SIGNOR; Q8N0X7; -.
DR BioGRID-ORCS; 23111; 11 hits in 1092 CRISPR screens.
DR ChiTaRS; SPG20; human.
DR EvolutionaryTrace; Q8N0X7; -.
DR GeneWiki; SPG20; -.
DR GenomeRNAi; 23111; -.
DR Pharos; Q8N0X7; Tbio.
DR PRO; PR:Q8N0X7; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q8N0X7; protein.
DR Bgee; ENSG00000133104; Expressed in calcaneal tendon and 200 other tissues.
DR ExpressionAtlas; Q8N0X7; baseline and differential.
DR Genevisible; Q8N0X7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005811; C:lipid droplet; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0009838; P:abscission; IMP:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0030509; P:BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR GO; GO:0048669; P:collateral sprouting in absence of injury; IEA:Ensembl.
DR GO; GO:0034389; P:lipid droplet organization; IEA:Ensembl.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR GO; GO:0048698; P:negative regulation of collateral sprouting in absence of injury; IEA:Ensembl.
DR GO; GO:0050905; P:neuromuscular process; IEA:Ensembl.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:MGI.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR009686; Senescence/spartin_C.
DR InterPro; IPR045036; Spartin-like.
DR PANTHER; PTHR21068; PTHR21068; 1.
DR Pfam; PF06911; Senescence; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Disease variant;
KW Hereditary spastic paraplegia; Isopeptide bond; Neurodegeneration;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..666
FT /note="Spartin"
FT /id="PRO_0000072119"
FT DOMAIN 16..94
FT /note="MIT"
FT DOMAIN 427..611
FT /note="Senescence"
FT /evidence="ECO:0000255"
FT REGION 124..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 646..666
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 362
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:19580544"
FT VARIANT 330
FT /note="M -> V (in SPG20; significant decrease in protein
FT expression; significantly reduced COX respiratory chain
FT complex IV activity in muscle mitochondria;
FT dbSNP:rs1399213398)"
FT /evidence="ECO:0000269|PubMed:27539578"
FT /id="VAR_079569"
FT VARIANT 442
FT /note="A -> P (in SPG20; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28875386"
FT /id="VAR_079570"
FT MUTAGEN 24
FT /note="F->D: Abolishes interaction with IST1. Does not
FT localize to the midbody."
FT /evidence="ECO:0000269|PubMed:20719964"
FT MUTAGEN 171..174
FT /note="PPAY->AAAA: Abolishes interaction with ITCH and
FT WWP1."
FT /evidence="ECO:0000269|PubMed:19580544"
FT CONFLICT 69
FT /note="P -> T (in Ref. 5; AAH47083)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="P -> H (in Ref. 5; AAH47083)"
FT /evidence="ECO:0000305"
FT HELIX 11..35
FT /evidence="ECO:0007829|PDB:4U7I"
FT HELIX 39..57
FT /evidence="ECO:0007829|PDB:4U7I"
FT HELIX 69..96
FT /evidence="ECO:0007829|PDB:4U7I"
SQ SEQUENCE 666 AA; 72833 MW; CFC8DF65494427CE CRC64;
MEQEPQNGEP AEIKIIREAY KKAFLFVNKG LNTDELGQKE EAKNYYKQGI GHLLRGISIS
SKESEHTGPG WESARQMQQK MKETLQNVRT RLEILEKGLA TSLQNDLQEV PKLYPEFPPK
DMCEKLPEPQ SFSSAPQHAE VNGNTSTPSA GAVAAPASLS LPSQSCPAEA PPAYTPQAAE
GHYTVSYGTD SGEFSSVGEE FYRNHSQPPP LETLGLDADE LILIPNGVQI FFVNPAGEVS
APSYPGYLRI VRFLDNSLDT VLNRPPGFLQ VCDWLYPLVP DRSPVLKCTA GAYMFPDTML
QAAGCFVGVV LSSELPEDDR ELFEDLLRQM SDLRLQANWN RAEEENEFQI PGRTRPSSDQ
LKEASGTDVK QLDQGNKDVR HKGKRGKRAK DTSSEEVNLS HIVPCEPVPE EKPKELPEWS
EKVAHNILSG ASWVSWGLVK GAEITGKAIQ KGASKLRERI QPEEKPVEVS PAVTKGLYIA
KQATGGAAKV SQFLVDGVCT VANCVGKELA PHVKKHGSKL VPESLKKDKD GKSPLDGAMV
VAASSVQGFS TVWQGLECAA KCIVNNVSAE TVQTVRYKYG YNAGEATHHA VDSAVNVGVT
AYNINNIGIK AMVKKTATQT GHTLLEDYQI VDNSQRENQE GAANVNVRGE KDEQTKEVKE
AKKKDK
